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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
1997-5-2
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pubmed:abstractText |
Fas (APO-1/CD95), which is a member of the tumor necrosis factor receptor superfamily, is a cell surface receptor that induces apoptosis. A protein tyrosine phosphatase, Fas-associated phosphatase-1 (FAP-1), that was previously identified as a Fas binding protein interacts with the C-terminal 15 amino acids of the regulatory domain of the Fas receptor. To identify the minimal region of the Fas C-terminal necessary for binding to FAP-1, we employed an in vitro inhibition assay of Fas/FAP-1 binding using a series of synthetic peptides as well as a screen of random peptide libraries by the yeast two-hybrid system. The results showed that the C-terminal three amino acids (SLV) of human Fas were necessary and sufficient for its interaction with the third PDZ (GLGF) domain of FAP-1. Furthermore, the direct cytoplasmic microinjection of this tripeptide (Ac-SLV) resulted in the induction of Fas-mediated apoptosis in a colon cancer cell line that expresses both Fas and FAP-1. Since t(S/T)X(V/L/I) motifs in the C termini of several other receptors have been shown to interact with PDZ domain in signal transducing molecules, this may represent a general motif for protein-protein interactions with important biological functions.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FAF1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Faf1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN13 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, N-Methyl-D-Aspartate,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:KamishoharaMM,
pubmed-author:KankeLL,
pubmed-author:KataokaSS,
pubmed-author:KobayashiEE,
pubmed-author:NishitobaTT,
pubmed-author:SatoTT,
pubmed-author:SawaEE,
pubmed-author:TakahashiMM,
pubmed-author:TazunokiTT,
pubmed-author:YanagisawaJJ,
pubmed-author:Yano-YanagisawaHH
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pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8539-45
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pubmed:dateRevised |
2008-5-21
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pubmed:meshHeading |
pubmed-meshheading:9079683-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:9079683-Alternative Splicing,
pubmed-meshheading:9079683-Amino Acid Sequence,
pubmed-meshheading:9079683-Animals,
pubmed-meshheading:9079683-Apoptosis,
pubmed-meshheading:9079683-Carrier Proteins,
pubmed-meshheading:9079683-Helix-Loop-Helix Motifs,
pubmed-meshheading:9079683-Humans,
pubmed-meshheading:9079683-Mice,
pubmed-meshheading:9079683-Microinjections,
pubmed-meshheading:9079683-Molecular Sequence Data,
pubmed-meshheading:9079683-Oligopeptides,
pubmed-meshheading:9079683-Peptide Mapping,
pubmed-meshheading:9079683-Potassium Channels,
pubmed-meshheading:9079683-Protein Phosphatase 1,
pubmed-meshheading:9079683-Protein Tyrosine Phosphatase, Non-Receptor Type 13,
pubmed-meshheading:9079683-Protein Tyrosine Phosphatases,
pubmed-meshheading:9079683-Rats,
pubmed-meshheading:9079683-Receptors, N-Methyl-D-Aspartate,
pubmed-meshheading:9079683-Transcription Factors,
pubmed-meshheading:9079683-Tumor Cells, Cultured
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pubmed:year |
1997
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pubmed:articleTitle |
The molecular interaction of Fas and FAP-1. A tripeptide blocker of human Fas interaction with FAP-1 promotes Fas-induced apoptosis.
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pubmed:affiliation |
Division of Molecular Oncology, Department of Otolaryngology/Head & Neck Surgery and Pathology, College of Physicians & Surgeons, Columbia University, New York, New York 10032, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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